Solution conformation of the type I collagen alpha-2 chain telopeptides studied by 1H and 13C NMR spectroscopy.
The high-field 1H and 13C NMR studies of the N- and C-terminal telopeptides of the alpha-2 chain of collagen were carried out in CD3OH/H2O solutions. All proton assignments are based on two-dimensional phase-sensitive COSY and ROESY experiments. The conformation of the N-telopeptide (nonamer) is predominantly extended with a small proportion of the molecules existing in a type I beta turn. The four residues involved in this turn are D3-A4-K5-G6 which is stabilized by a C = O(D3)-NH(G6) hydrogen bond. The C-terminal telopeptide is extended throughout. A model is proposed involving charge-charge and hydrophobic interactions between the extended alpha-2 chain N-telopeptide and the adjacent segments of triple-helix. A similar model is proposed for the C-telopeptide.
Liu
X H
XH
Department of Chemistry, University of Alberta, Edmonton, Canada.
Scott
P G
PG
Otter
A
A
Kotovych
G
G
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D003094:Collagen / Q000737:chemistry*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D000432:Methanol; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014867:Water
D002247:Carbon Isotopes; D014867:Water; D006859:Hydrogen; D003094:Collagen; D000432:Methanol